Kasuya_2003_Int.J.Biol.Macromol_33_221

Reference

Title : Cloning, expression and characterization of a poly(3-hydroxybutyrate) depolymerase from Marinobacter sp. NK-1 - Kasuya_2003_Int.J.Biol.Macromol_33_221
Author(s) : Kasuya K , Takano T , Tezuka Y , Hsieh WC , Mitomo H , Doi Y
Ref : Int J Biol Macromol , 33 :221 , 2003
Abstract :

A DNA fragment carrying the gene encoding poly(3-hydroxybutyrate) (P(3HB)) depolymerase was cloned from the genomic DNA of Marinobacter sp. DNA sequencing analysis revealed that the Marinobacter sp. P(3HB) depolymerase gene is composed of 1734bp and encodes 578 amino acids with a molecular mass of 61,757Da. A sequence homology search showed that the deduced protein contains the signal peptide, catalytic domain (CD), cadherin-type linker domain (LD), and two substrate-binding domain (SBD). The fusion proteins of glutathione S-transferase (GST) with the CD showed the hydrolytic activity for denatured P(3HB) (dP(3HB)), P(3HB) emulsion (eP(3HB)) and p-nitrophenylbutyrate. On the other hand, the fusion proteins lacking the SBD showed much lower hydrolytic activity for dP(3HB) compared to the proteins containing both CD and SBD. In addition, binding tests revealed that the SBDs are specifically bound not to eP(3HB) but dP(3HB). These suggest that the SBDs play a crucial role in the enzymatic hydrolysis of dP(3HB) that is a solid substrate.

PubMedSearch : Kasuya_2003_Int.J.Biol.Macromol_33_221
PubMedID: 14607367
Gene_locus related to this paper: marsp-PHAZ

Related information

Gene_locus marsp-PHAZ

Citations formats

Kasuya K, Takano T, Tezuka Y, Hsieh WC, Mitomo H, Doi Y (2003)
Cloning, expression and characterization of a poly(3-hydroxybutyrate) depolymerase from Marinobacter sp. NK-1
Int J Biol Macromol 33 :221

Kasuya K, Takano T, Tezuka Y, Hsieh WC, Mitomo H, Doi Y (2003)
Int J Biol Macromol 33 :221